FMO DATABASE

FMODB ID: ZG6LN

Calculation Name: 3EVX-A-Xray549

Preferred Name:

Target Type:

Ligand Name: thiocyanate ion

Ligand 3-letter code: SCN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3EVX

Chain ID: A

ChEMBL ID:

UniProt ID: Q9Y3C8

Base Structure: X-ray

Registration Date: 2025-10-12

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	158
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1647304.620893
FMO2-HF: Nuclear repulsion	1583542.616127
FMO2-HF: Total energy	-63762.004767
FMO2-MP2: Total energy	-63950.564844

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:5:ALA)

Summations of interaction energy for fragment #1(A:5:ALA)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
62.319	64.847	0.042	-0.938	-1.632	-0.003

Interaction energy analysis for fragmet #1(A:5:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.888 / q_NPA : 0.934

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	7	ARG	1	0.953	0.980	3.181	40.681	42.228	0.018	-0.667	-0.898	-0.002
4	A	8	ARG	1	0.864	0.945	3.170	54.503	55.323	0.025	-0.252	-0.594	-0.001
5	A	9	VAL	0	0.179	0.096	4.978	5.850	6.011	-0.001	-0.019	-0.140	0.000
6	A	10	VAL	0	-0.005	-0.017	7.278	4.758	4.758	0.000	0.000	0.000	0.000
7	A	11	SER	0	-0.087	-0.053	7.674	2.964	2.964	0.000	0.000	0.000	0.000
8	A	12	GLU	-1	-0.904	-0.945	7.943	-33.164	-33.164	0.000	0.000	0.000	0.000
9	A	13	ILE	0	-0.039	0.003	11.444	2.012	2.012	0.000	0.000	0.000	0.000
10	A	14	PRO	0	-0.017	0.008	13.730	0.181	0.181	0.000	0.000	0.000	0.000
11	A	15	VAL	0	-0.004	-0.014	15.907	0.246	0.246	0.000	0.000	0.000	0.000
12	A	16	LEU	0	-0.017	0.010	18.158	0.718	0.718	0.000	0.000	0.000	0.000
13	A	17	LYS	1	0.850	0.896	21.428	13.011	13.011	0.000	0.000	0.000	0.000
14	A	18	THR	0	-0.011	-0.019	24.516	0.557	0.557	0.000	0.000	0.000	0.000
15	A	19	ASN	0	-0.069	-0.047	25.710	-0.497	-0.497	0.000	0.000	0.000	0.000
16	A	20	ALA	0	0.044	0.020	27.352	0.402	0.402	0.000	0.000	0.000	0.000
17	A	21	GLY	0	0.078	0.049	28.174	-0.456	-0.456	0.000	0.000	0.000	0.000
18	A	22	PRO	0	-0.004	-0.013	29.027	0.228	0.228	0.000	0.000	0.000	0.000
19	A	23	ARG	1	0.916	0.952	31.385	8.520	8.520	0.000	0.000	0.000	0.000
20	A	24	ASP	-1	-0.861	-0.914	32.403	-9.396	-9.396	0.000	0.000	0.000	0.000
21	A	25	ARG	1	0.930	0.941	34.988	8.014	8.014	0.000	0.000	0.000	0.000
22	A	26	GLU	-1	-0.869	-0.929	35.263	-8.527	-8.527	0.000	0.000	0.000	0.000
23	A	27	LEU	0	0.018	0.007	31.864	-0.242	-0.242	0.000	0.000	0.000	0.000
24	A	28	TRP	0	-0.035	-0.007	26.794	-0.535	-0.535	0.000	0.000	0.000	0.000
25	A	29	VAL	0	0.041	0.020	30.602	-0.356	-0.356	0.000	0.000	0.000	0.000
26	A	30	GLN	0	-0.058	-0.027	28.953	0.070	0.070	0.000	0.000	0.000	0.000
27	A	31	ARG	1	0.726	0.842	21.332	13.466	13.466	0.000	0.000	0.000	0.000
28	A	32	LEU	0	0.013	0.016	26.177	-0.624	-0.624	0.000	0.000	0.000	0.000
29	A	33	LYS	1	0.946	0.974	26.802	10.071	10.071	0.000	0.000	0.000	0.000
30	A	34	GLU	-1	-0.763	-0.852	23.904	-12.897	-12.897	0.000	0.000	0.000	0.000
31	A	35	GLU	-1	-0.702	-0.827	21.274	-15.573	-15.573	0.000	0.000	0.000	0.000
32	A	36	TYR	0	0.018	-0.008	21.949	-0.648	-0.648	0.000	0.000	0.000	0.000
33	A	37	GLN	0	-0.043	-0.024	22.683	-0.018	-0.018	0.000	0.000	0.000	0.000
34	A	38	SER	0	-0.020	-0.021	18.049	-0.898	-0.898	0.000	0.000	0.000	0.000
35	A	39	LEU	0	0.002	-0.003	17.900	-1.155	-1.155	0.000	0.000	0.000	0.000
36	A	40	ILE	0	0.008	0.007	18.520	-0.682	-0.682	0.000	0.000	0.000	0.000
37	A	41	ARG	1	0.892	0.938	15.945	17.950	17.950	0.000	0.000	0.000	0.000
38	A	42	TYR	0	0.016	0.016	10.378	-0.506	-0.506	0.000	0.000	0.000	0.000
39	A	43	VAL	0	0.011	0.009	14.401	-1.104	-1.104	0.000	0.000	0.000	0.000
40	A	44	GLU	-1	-0.844	-0.923	16.474	-16.004	-16.004	0.000	0.000	0.000	0.000
41	A	45	ASN	0	0.002	0.012	11.742	1.261	1.261	0.000	0.000	0.000	0.000
42	A	46	ASN	0	0.006	-0.011	11.507	-3.281	-3.281	0.000	0.000	0.000	0.000
43	A	47	LYS	1	0.841	0.921	12.974	15.466	15.466	0.000	0.000	0.000	0.000
44	A	48	ASN	0	-0.086	-0.045	13.938	0.358	0.358	0.000	0.000	0.000	0.000
45	A	49	ALA	0	-0.041	-0.017	9.520	-0.129	-0.129	0.000	0.000	0.000	0.000
46	A	50	ASP	-1	-0.950	-0.958	11.273	-20.697	-20.697	0.000	0.000	0.000	0.000
47	A	51	ASN	0	-0.018	-0.006	10.012	-0.455	-0.455	0.000	0.000	0.000	0.000
48	A	52	ASP	-1	-0.804	-0.884	12.676	-17.296	-17.296	0.000	0.000	0.000	0.000
49	A	53	TRP	0	0.019	0.016	12.138	1.106	1.106	0.000	0.000	0.000	0.000
50	A	54	PHE	0	-0.010	-0.002	15.539	0.539	0.539	0.000	0.000	0.000	0.000
51	A	55	ARG	1	0.783	0.853	18.445	15.420	15.420	0.000	0.000	0.000	0.000
52	A	56	LEU	0	-0.034	-0.019	20.807	0.016	0.016	0.000	0.000	0.000	0.000
53	A	57	GLU	-1	-0.922	-0.946	23.050	-11.229	-11.229	0.000	0.000	0.000	0.000
54	A	58	SER	0	0.027	0.005	26.596	-0.237	-0.237	0.000	0.000	0.000	0.000
55	A	59	ASN	0	0.024	0.014	29.004	0.052	0.052	0.000	0.000	0.000	0.000
56	A	60	LYS	1	0.962	0.962	32.009	8.016	8.016	0.000	0.000	0.000	0.000
57	A	61	GLU	-1	-0.904	-0.943	33.858	-8.962	-8.962	0.000	0.000	0.000	0.000
58	A	62	GLY	0	0.051	0.036	29.557	-0.132	-0.132	0.000	0.000	0.000	0.000
59	A	63	THR	0	-0.011	0.000	28.807	-0.419	-0.419	0.000	0.000	0.000	0.000
60	A	64	ARG	1	0.829	0.908	29.425	9.642	9.642	0.000	0.000	0.000	0.000
61	A	65	TRP	0	-0.013	-0.026	24.537	-0.081	-0.081	0.000	0.000	0.000	0.000
62	A	66	PHE	0	0.030	0.021	26.297	0.054	0.054	0.000	0.000	0.000	0.000
63	A	67	GLY	0	0.033	0.007	23.892	-0.208	-0.208	0.000	0.000	0.000	0.000
64	A	68	LYS	1	0.854	0.931	22.782	12.457	12.457	0.000	0.000	0.000	0.000
65	A	69	CYS	0	-0.069	-0.020	17.469	-0.750	-0.750	0.000	0.000	0.000	0.000
66	A	70	TRP	0	0.006	-0.013	17.876	1.009	1.009	0.000	0.000	0.000	0.000
67	A	71	TYR	0	0.005	0.007	12.350	-1.778	-1.778	0.000	0.000	0.000	0.000
68	A	72	ILE	0	-0.029	-0.017	15.810	1.177	1.177	0.000	0.000	0.000	0.000
69	A	73	HIS	0	-0.020	-0.015	16.338	-1.682	-1.682	0.000	0.000	0.000	0.000
70	A	74	ASP	-1	-0.854	-0.934	18.700	-14.056	-14.056	0.000	0.000	0.000	0.000
71	A	75	LEU	0	-0.030	-0.025	19.884	0.701	0.701	0.000	0.000	0.000	0.000
72	A	76	LEU	0	-0.013	0.019	21.400	0.161	0.161	0.000	0.000	0.000	0.000
73	A	77	LYS	1	0.950	0.976	20.286	13.576	13.576	0.000	0.000	0.000	0.000
74	A	78	TYR	0	0.017	0.005	20.400	0.935	0.935	0.000	0.000	0.000	0.000
75	A	79	GLU	-1	-0.930	-0.982	20.476	-13.837	-13.837	0.000	0.000	0.000	0.000
76	A	80	PHE	0	0.020	0.006	19.941	0.296	0.296	0.000	0.000	0.000	0.000
77	A	81	ASP	-1	-0.834	-0.909	22.804	-11.947	-11.947	0.000	0.000	0.000	0.000
78	A	82	ILE	0	-0.071	-0.046	19.708	-0.385	-0.385	0.000	0.000	0.000	0.000
79	A	83	GLU	-1	-0.934	-0.972	23.661	-10.749	-10.749	0.000	0.000	0.000	0.000
80	A	84	PHE	0	-0.025	-0.026	21.358	-0.526	-0.526	0.000	0.000	0.000	0.000
81	A	85	ASP	-1	-0.766	-0.870	25.338	-10.115	-10.115	0.000	0.000	0.000	0.000
82	A	86	ILE	0	-0.057	-0.028	24.835	-0.470	-0.470	0.000	0.000	0.000	0.000
83	A	87	PRO	0	-0.002	0.000	25.064	0.486	0.486	0.000	0.000	0.000	0.000
84	A	88	ILE	0	0.031	0.000	28.125	-0.082	-0.082	0.000	0.000	0.000	0.000
85	A	89	THR	0	0.006	-0.010	27.694	0.175	0.175	0.000	0.000	0.000	0.000
86	A	90	TYR	0	-0.069	-0.029	21.697	-0.670	-0.670	0.000	0.000	0.000	0.000
87	A	91	PRO	0	0.041	0.010	22.694	0.363	0.363	0.000	0.000	0.000	0.000
88	A	92	THR	0	-0.006	-0.020	22.466	-0.731	-0.731	0.000	0.000	0.000	0.000
89	A	93	THR	0	-0.071	-0.025	22.875	-0.270	-0.270	0.000	0.000	0.000	0.000
90	A	94	ALA	0	-0.002	-0.007	18.847	0.165	0.165	0.000	0.000	0.000	0.000
91	A	95	PRO	0	0.017	-0.003	20.541	0.342	0.342	0.000	0.000	0.000	0.000
92	A	96	GLU	-1	-0.858	-0.897	20.698	-12.442	-12.442	0.000	0.000	0.000	0.000
93	A	97	ILE	0	-0.023	-0.008	16.899	0.343	0.343	0.000	0.000	0.000	0.000
94	A	98	ALA	0	0.011	0.014	21.223	0.033	0.033	0.000	0.000	0.000	0.000
95	A	99	VAL	0	0.027	0.009	20.892	-0.286	-0.286	0.000	0.000	0.000	0.000
96	A	100	PRO	0	0.047	0.019	23.730	0.072	0.072	0.000	0.000	0.000	0.000
97	A	101	GLU	-1	-0.848	-0.917	25.885	-11.584	-11.584	0.000	0.000	0.000	0.000
98	A	102	LEU	0	-0.026	-0.015	21.466	0.104	0.104	0.000	0.000	0.000	0.000
99	A	103	ASP	-1	-0.828	-0.927	25.612	-10.711	-10.711	0.000	0.000	0.000	0.000
100	A	104	GLY	0	-0.061	-0.024	27.678	0.291	0.291	0.000	0.000	0.000	0.000
101	A	105	LYS	1	0.852	0.933	26.016	11.244	11.244	0.000	0.000	0.000	0.000
102	A	106	THR	0	0.009	-0.014	20.489	-0.091	-0.091	0.000	0.000	0.000	0.000
103	A	107	ALA	0	-0.004	-0.001	23.674	0.125	0.125	0.000	0.000	0.000	0.000
104	A	108	LYS	1	0.773	0.887	17.423	15.750	15.750	0.000	0.000	0.000	0.000
105	A	109	MET	0	0.000	0.002	19.570	-0.924	-0.924	0.000	0.000	0.000	0.000
106	A	110	TYR	0	-0.029	-0.010	22.106	0.456	0.456	0.000	0.000	0.000	0.000
107	A	111	ARG	1	0.947	0.955	25.031	9.442	9.442	0.000	0.000	0.000	0.000
108	A	112	GLY	0	0.011	0.009	27.775	-0.102	-0.102	0.000	0.000	0.000	0.000
109	A	113	GLY	0	0.026	0.011	25.288	-0.123	-0.123	0.000	0.000	0.000	0.000
110	A	114	LYS	1	0.835	0.908	23.464	10.956	10.956	0.000	0.000	0.000	0.000
111	A	115	ILE	0	0.013	0.002	16.729	-0.097	-0.097	0.000	0.000	0.000	0.000
112	A	116	CYS	0	-0.054	-0.009	18.517	0.384	0.384	0.000	0.000	0.000	0.000
113	A	117	LEU	0	-0.029	-0.003	13.588	-0.695	-0.695	0.000	0.000	0.000	0.000
114	A	118	THR	0	0.043	0.020	11.414	0.673	0.673	0.000	0.000	0.000	0.000
115	A	119	ASP	-1	-0.848	-0.930	14.404	-16.657	-16.657	0.000	0.000	0.000	0.000
116	A	120	HIS	0	-0.029	-0.027	11.647	-0.594	-0.594	0.000	0.000	0.000	0.000
117	A	121	PHE	0	-0.005	0.011	12.264	-0.516	-0.516	0.000	0.000	0.000	0.000
118	A	122	LYS	1	0.986	0.998	13.596	14.709	14.709	0.000	0.000	0.000	0.000
119	A	123	PRO	0	0.029	-0.004	15.996	0.289	0.289	0.000	0.000	0.000	0.000
120	A	124	LEU	0	-0.064	-0.028	9.934	0.063	0.063	0.000	0.000	0.000	0.000
121	A	125	TRP	0	0.007	0.001	14.276	-0.641	-0.641	0.000	0.000	0.000	0.000
122	A	126	ALA	0	0.022	0.012	16.492	0.460	0.460	0.000	0.000	0.000	0.000
123	A	127	ARG	1	0.921	0.967	12.817	19.667	19.667	0.000	0.000	0.000	0.000
124	A	128	ASN	0	-0.075	-0.045	13.751	-0.220	-0.220	0.000	0.000	0.000	0.000
125	A	129	VAL	0	-0.005	0.041	17.605	0.044	0.044	0.000	0.000	0.000	0.000
126	A	130	PRO	0	-0.021	-0.020	20.969	0.213	0.213	0.000	0.000	0.000	0.000
127	A	131	LYS	1	0.979	0.988	17.110	17.166	17.166	0.000	0.000	0.000	0.000
128	A	132	PHE	0	-0.004	0.002	11.843	-1.030	-1.030	0.000	0.000	0.000	0.000
129	A	133	GLY	0	0.072	0.029	17.271	1.176	1.176	0.000	0.000	0.000	0.000
130	A	134	LEU	0	-0.011	-0.001	17.443	-1.085	-1.085	0.000	0.000	0.000	0.000
131	A	135	ALA	0	0.047	0.030	15.788	-0.558	-0.558	0.000	0.000	0.000	0.000
132	A	136	HIS	0	0.015	0.007	12.939	-0.847	-0.847	0.000	0.000	0.000	0.000
133	A	137	LEU	0	-0.007	-0.006	12.926	-1.458	-1.458	0.000	0.000	0.000	0.000
134	A	138	MET	0	-0.009	0.016	14.603	-0.286	-0.286	0.000	0.000	0.000	0.000
135	A	139	ALA	0	0.000	0.002	9.822	-0.948	-0.948	0.000	0.000	0.000	0.000
136	A	140	LEU	0	-0.101	-0.067	7.912	-3.607	-3.607	0.000	0.000	0.000	0.000
137	A	141	GLY	0	0.004	0.004	10.312	0.092	0.092	0.000	0.000	0.000	0.000
138	A	142	LEU	0	0.059	0.014	12.970	-0.410	-0.410	0.000	0.000	0.000	0.000
139	A	143	GLY	0	0.024	0.032	10.927	0.177	0.177	0.000	0.000	0.000	0.000
140	A	144	PRO	0	-0.069	-0.052	7.684	-0.742	-0.742	0.000	0.000	0.000	0.000
141	A	145	TRP	0	0.017	0.014	9.690	0.265	0.265	0.000	0.000	0.000	0.000
142	A	146	LEU	0	0.017	-0.001	13.273	0.842	0.842	0.000	0.000	0.000	0.000
143	A	147	ALA	0	-0.005	-0.006	9.840	0.715	0.715	0.000	0.000	0.000	0.000
144	A	148	VAL	0	-0.050	-0.009	10.961	-0.015	-0.015	0.000	0.000	0.000	0.000
145	A	149	GLU	-1	-0.750	-0.869	13.448	-15.299	-15.299	0.000	0.000	0.000	0.000
146	A	150	ILE	0	-0.010	0.010	16.299	0.970	0.970	0.000	0.000	0.000	0.000
147	A	151	PRO	0	0.031	0.022	14.319	1.013	1.013	0.000	0.000	0.000	0.000
148	A	152	ASP	-1	-0.821	-0.887	17.457	-13.988	-13.988	0.000	0.000	0.000	0.000
149	A	153	LEU	0	-0.009	-0.019	19.201	0.910	0.910	0.000	0.000	0.000	0.000
150	A	154	ILE	0	-0.006	0.009	19.595	0.680	0.680	0.000	0.000	0.000	0.000
151	A	155	GLN	0	-0.061	-0.026	19.461	0.648	0.648	0.000	0.000	0.000	0.000
152	A	156	LYS	1	0.770	0.865	21.235	14.294	14.294	0.000	0.000	0.000	0.000
153	A	157	GLY	0	-0.004	0.010	25.327	0.468	0.468	0.000	0.000	0.000	0.000
154	A	158	VAL	0	-0.046	-0.012	25.180	0.399	0.399	0.000	0.000	0.000	0.000
155	A	159	ILE	0	-0.057	-0.032	22.626	0.236	0.236	0.000	0.000	0.000	0.000
156	A	160	GLN	0	0.003	-0.003	25.759	0.021	0.021	0.000	0.000	0.000	0.000
157	A	161	HIS	0	-0.015	-0.016	24.439	0.171	0.171	0.000	0.000	0.000	0.000
158	A	162	LYS	0	0.033	0.031	27.294	-0.805	-0.805	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:ALA)